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==Fibrinogen 3GHG ==
==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='3GHG' size='340' side='right' caption='Caption for this structure' scene='78/781216/Origfibri/1''>
<StructureSection load='3VEV' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.


== Structure ==
Fibrinogen is located in the circulatory system as part of plasma, it is readily available.
Fibrinogen is a ~340KD glycoprotein made up of two subunits which include <scene name='78/781216/Abysubunitsrbg/5'>three non-identical chains</scene>  Aα, Bβ γ. Its central region also called “E region” is where all chains meet, the chains intertwine with each other to hold both of the subunits together. At the ends of the a and b chains are fibrinopeptides, fibrinopeptide A is about 16 amino acids long, while fibrinopeptide B is around 15 amino acids long. These small peptides become very important when activating fibrinogen. On both ends of fibrinogen are the D regions containing the β & γ nodule and the coiled-coil region.
== Function ==
== Function ==
Fibrinogen is an essential protein in coagulation, which is initiated through either an intrinsic or extrinsic pathway. Both pathways trigger a cascade of reactions that lead to the formation of a blood clot. At some point the protease thrombin is activated, thrombin then converts fibrinogen to fibrin. It does this by cleaving both the <scene name='78/781216/Fribrinopeptide_a_and_b/3'>fibrinopeptide A and B</scene> off of the amino terminus of the alpha and beta chains. The alpha and beta knobs will bind to <scene name='78/781216/Aandb_modules/1'>a and b holes</scene> of other fibrin molecules making fibrin mesh strong enough to hold the platelet plug.


== Disease ==
== Disease ==
'''Congenital Afibrinogenemia''' – a genetic disorder that results in the lack of fibrinogen which causes abnormal bleeding including gastrointestinal hemorrhage, cutaneous bleeding, etc.
'''Hepatic fibrinogen storage disease''' - occurs when there is a mutation in the γ chain which causes the storage of fibrinogen in the ER of liver cells. The storage of fibrinogen in these cells can cause liver disease.
'''Acquired Dysfibrinogenemia''' - may occur as a result of liver disease which causes an error during fibrinogen synthesis resulting in dysfunctional fibrinogen


== Relevance ==


== Structural highlights ==
== Structural highlights ==


<scene name='78/781216/Abysubunitsrbg/5'>three non-identical chains</scene>
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
 
<scene name='78/781216/Fribrinopeptide_a_and_b/3'>fibrinopeptide A and B</scene>
 
<scene name='78/781216/Aandb_modules/1'>a and b holes</scene>
 
<scene name='78/781216/Origfibri/1'>Fibrinogen</scene>


This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
</StructureSection>
</StructureSection>
== References ==
== References ==
 
<references/>
1. Acharya, S. S., & Dimichele, D. M. (2008). Rare inherited disorders of fibrinogen. Haemophilia, 14(6), 1151–1158. doi: 10.1111/j.1365-2516.2008.01831.x
 
2. Al-Hussaini, A., Altalhi, A., Hag, I. E., Alhussaini, H., Francalanci, P., Giovannoni, I., & Callea, F. (2014). Hepatic fibrinogen storage disease due to the fibrinogen γ375 Arg → Trp mutation "fibrinogen aguadilla" is present in Arabs. Saudi Journal of Gastroenterology, 20(4), 255. doi: 10.4103/1319-3767.136985
 
3. Doolittle, R., Kollman, J., Sawaya, M., Pandi, L., & Riley, M. (2009). Crystal Structure of Human Fibrinogen. American Chemical Society. doi: 10.2210/pdb3ghg/pdb
 
4. Köhler, S., Schmid, F., & Settanni, G. (2015). The Internal Dynamics of Fibrinogen and Its Implications for Coagulation and Adsorption. PLOS Computational Biology, 11(9). doi: 10.1371/journal.pcbi.1004346
 
5. Medved, L., & Weisel, J. W. (2009). Recommendations for nomenclature on fibrinogen and fibrin. Journal of Thrombosis and Haemostasis, 7(2), 355–359. doi: 10.1111/j.1538-7836.2008.03242.x

Revision as of 18:20, 10 February 2021

Your Heading Here (maybe something like 'Structure')Your Heading Here (maybe something like 'Structure')

This is a default text for your page. Click above on edit this page to modify. Be careful with the < and > signs.

You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.

Function

Disease

Relevance

Structural highlights

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.


Caption for this structure

Drag the structure with the mouse to rotate

ReferencesReferences

  1. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Student, James Nolan